Urotensin I and its N-terminal flanking peptide from the flounder, Platichthys flesus.
The caudal spinal cord region of teleost fish terminates in a neurosecretory organ, the urophysis. Two peptides have been purified to homogeneity from an extract of the urophysis of a teleost fish, the flounder. The primary structure of one peptide, Ser-Glu-Asp-Pro-Pro-Met-Ser-Ile-Asp-Leu10-Thr-Phe-His-Met-Leu-Arg- Asn-Met-Ile- His20-Met-Ala-Lys-Met-Glu-Gly-Glu-Arg-Glu-Gln30-Ala-Gln-Ile- Asn-Arg-Asn-Leu-Leu - Asp-Glu40-Val, indicates identity with urotensin I. By analogy with other urotensins, the COOH-terminal residue is probably alpha-amidated. A second peptide was present in the extract in a concentration that was approximately equimolar with that of urotensin I. The amino acid composition of this peptide indicated a total of approximately 65 residues. The amino acid sequence of a fragment produced by digestion with trypsin was established as: Ala-Ala-Ala-Ala-Gly5-Asp-Ser-Ala-Ala-Ser10-Asp-Leu-Leu-Gly-Asp1 5-Asn-Ile-Leu- Arg. This sequence shows partial homology to carp prepro-urotensin I(41-59)-peptide as deduced from the nucleotide sequence of a cloned cDNA. It is concluded that the second peptide probably represents the N-terminal flanking peptide of pro-urotensin I which, it has previously been suggested, may function as a urotensin-binding peptide (urophysin) analogous to the neurophysins.
Conlon
J M
JM
Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68178.
Arnold-Reed
D E
DE
Balment
R J
RJ
D000595:Amino Acid Sequence; D000818:Animals; D005399:Fishes / Q000235:genetics; D005432:Flounder / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009490:Neurosecretory Systems / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D014579:Urotensins / Q000235:genetics / Q000302:isolation & purification*
D014579:Urotensins; C029676:urotensin I